This project is concerned with determining the secondary and tertiary structure of the winter flounder antifreeze molecule (HPLC-6). Specifically, whether the (-helical chain of the peptide is bent in solution. Our computer simulations of the peptide in SPC and TIP3 water predicted a 40x-50x bend in the middle of the peptide. Recent X-ray crystallographic work has added to our prediction by showing that the peptide is bent as a crystal. The aim of the NMR analysis is to determine if the peptide is bent in solution and to confirm the CD work which showed that the peptide was (-helical in solution. Information on side chain conformations is also sought to better understand the peptide's ice binding properties.